The Amylases of Insects.

Jean-Luc Da Lage
{"title":"The Amylases of Insects.","authors":"Jean-Luc Da Lage","doi":"10.1177/1179543318804783","DOIUrl":null,"url":null,"abstract":"<p><p>Alpha-amylases are major digestive enzymes that act in the first step of maltopolysaccharide digestion. In insects, these enzymes have long been studied for applied as well as purely scientific purposes. In many species, amylases are produced by multiple gene copies. Rare species are devoid of <i>Amy</i> gene. They are predominantly secreted in the midgut but salivary expression is also frequent, with extraoral activity. Enzymological parameters are quite variable among insects, with visible trends according to phylogeny: Coleopteran amylases have acidic optimum activity, whereas dipteran amylases have neutral preference and lepidopteran ones have clear alkaline preference. The enzyme structure shows interesting variations shaped by evolutionary convergences, such as the recurrent loss of a loop involved in substrate handling. Many works have focused on the action of plant amylase inhibitors on pest insect amylases, in the frame of crop protection by transgenesis. It appears that sensitivity or resistance to inhibitors is finely tuned and very specific and that amylases and their inhibitors have coevolved. The multicopy feature of insect amylases appears to allow tissue-specific or stage-specific regulation, but also to broaden enzymological abilities, such as pH range, and to overcome plant inhibitory defenses.</p>","PeriodicalId":73456,"journal":{"name":"International journal of insect science","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2018-10-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1177/1179543318804783","citationCount":"45","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International journal of insect science","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1177/1179543318804783","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 45

Abstract

Alpha-amylases are major digestive enzymes that act in the first step of maltopolysaccharide digestion. In insects, these enzymes have long been studied for applied as well as purely scientific purposes. In many species, amylases are produced by multiple gene copies. Rare species are devoid of Amy gene. They are predominantly secreted in the midgut but salivary expression is also frequent, with extraoral activity. Enzymological parameters are quite variable among insects, with visible trends according to phylogeny: Coleopteran amylases have acidic optimum activity, whereas dipteran amylases have neutral preference and lepidopteran ones have clear alkaline preference. The enzyme structure shows interesting variations shaped by evolutionary convergences, such as the recurrent loss of a loop involved in substrate handling. Many works have focused on the action of plant amylase inhibitors on pest insect amylases, in the frame of crop protection by transgenesis. It appears that sensitivity or resistance to inhibitors is finely tuned and very specific and that amylases and their inhibitors have coevolved. The multicopy feature of insect amylases appears to allow tissue-specific or stage-specific regulation, but also to broaden enzymological abilities, such as pH range, and to overcome plant inhibitory defenses.

Abstract Image

Abstract Image

Abstract Image

昆虫淀粉酶。
α淀粉酶是在麦芽多糖消化的第一步中起作用的主要消化酶。在昆虫中,这些酶长期以来一直被研究用于应用和纯粹的科学目的。在许多物种中,淀粉酶是由多个基因拷贝产生的。稀有物种缺乏Amy基因。它们主要在中肠分泌,但唾液表达也很频繁,具有口外活动。昆虫之间的酶学参数变化很大,根据系统发育有明显的趋势:鞘翅目淀粉酶具有酸性最适活性,而二叶目淀粉酶具有中性偏好,鳞翅目淀粉酶有明显的碱性偏好。酶的结构显示出由进化收敛形成的有趣的变化,例如底物处理中循环的反复丢失。在转基因保护作物的框架内,许多工作都集中在植物淀粉酶抑制剂对害虫淀粉酶的作用上。似乎对抑制剂的敏感性或耐药性是精细调节的,并且是非常特异的,淀粉酶及其抑制剂已经共同进化。昆虫淀粉酶的多拷贝特性似乎允许组织特异性或阶段特异性调节,但也可以拓宽酶学能力,如pH范围,并克服植物的抑制性防御。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信